ID CAIA_SHIFL Reviewed; 380 AA. AC P60587; P31571; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 1. DT 02-SEP-2026, entry version 138. DE RecName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052}; DE EC=1.3.8.13 {ECO:0000255|HAMAP-Rule:MF_01052}; DE AltName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052}; GN Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052}; GN OrderedLocusNames=SF0036, S0038; OS Shigella flexneri. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma- CC butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-(trimethylamino)butanoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = crotonobetainyl-CoA + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:51584, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:60933, ChEBI:CHEBI:61513; EC=1.3.8.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01052}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01052}; CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01052}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01052}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01052}. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01052}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005674; AAN41702.1; -; Genomic_DNA. DR EMBL; AE014073; AAP15583.1; -; Genomic_DNA. DR RefSeq; NP_705995.1; NC_004337.2. DR RefSeq; WP_000347117.1; NZ_AP040250.1. DR AlphaFoldDB; P60587; -. DR SMR; P60587; -. DR STRING; 198214.SF0036; -. DR PaxDb; 198214-SF0036; -. DR GeneID; 1024569; -. DR GeneID; 93777396; -. DR KEGG; sfl:SF0036; -. DR KEGG; sfx:S0038; -. DR PATRIC; fig|198214.7.peg.42; -. DR HOGENOM; CLU_018204_0_2_6; -. DR UniPathway; UPA00117; -. DR Proteomes; UP000001006; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00567; ACAD; 1. DR FunFam; 1.20.140.10:FF:000001; Acyl-CoA dehydrogenase; 1. DR FunFam; 2.40.110.10:FF:000002; Acyl-CoA dehydrogenase fadE12; 1. DR FunFam; 1.10.540.10:FF:000005; Crotonobetainyl-CoA reductase; 1. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR HAMAP; MF_01052; CaiA; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR006091; AcylCoA_DH/ox_M. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR InterPro; IPR023450; CaiA. DR NCBIfam; NF002885; PRK03354.1; 1. DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1. DR PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR PIRSF; PIRSF016578; HsaA; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 3: Inferred from homology; KW Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome. FT CHAIN 1..380 FT /note="Crotonobetainyl-CoA reductase" FT /id="PRO_0000201199" SQ SEQUENCE 380 AA; 42558 MW; 7076984D735652C3 CRC64; MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH GGLDAGFVTL AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW NSAITEPGAG SDVGSLKTTY TRRNGKIYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE RFLVALTNYG TAMCAFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLYEA AWKADNGTIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGNHRISRF WRDLRVDRVS GGSDEMQILT LGRAVLKQYR //